Dual role of the serine protease homolog BmSPH-1 in the development and immunity of the silkworm Bombyx mori. (August 2018)
- Record Type:
- Journal Article
- Title:
- Dual role of the serine protease homolog BmSPH-1 in the development and immunity of the silkworm Bombyx mori. (August 2018)
- Main Title:
- Dual role of the serine protease homolog BmSPH-1 in the development and immunity of the silkworm Bombyx mori
- Authors:
- Lee, Kwang Sik
Kim, Bo Yeon
Choo, Young Moo
Jin, Byung Rae - Abstract:
- Abstract: Serine proteases and serine protease homologs are involved in the prophenoloxidase (proPO)-activating system leading to melanization. The Bombyx mori serine protease homolog BmSPH-1 regulates nodule melanization. Here, we show the dual role of BmSPH-1 in the development and immunity of B. mori . BmSPH-1 was expressed in hemocytes after molting and during the larval-pupal transformation in normal development. In contrast, following infection, BmSPH-1 was expressed in hemocytes and cleaved in the hemolymph, which resulted in the induction of PO activity. Moreover, BmSPH-1 was cleaved in the cuticle during the larval-pupal transformation and early pupal stages. In BmSPH-1 RNAi-treated silkworms, the reduced BmSPH-1 mRNA levels during the spinning stage or the prepupal stage resulted in the arrest of pupation or pupal cuticular melanization, respectively. The binding assays revealed that BmSPH-1 interacts with B. mori immulectin, proPO, and proPO-activating enzyme. Our findings demonstrate that BmSPH-1 paticipates larval-pupal transformation, pupal cuticular melanization and innate immunity of silkworms, illustrating the dual role of BmSPH-1 in development and immunity. Highlights: Bombyx mori serine protease homolog BmSPH-1 functions in both development and immunity. BmSPH-1 acts in the immune response during infection. BmSPH-1 is required for pupation during the larval-pupal transformation. BmSPH-1 participates in pupal cuticular melanization. BmSPH-1 interacts withAbstract: Serine proteases and serine protease homologs are involved in the prophenoloxidase (proPO)-activating system leading to melanization. The Bombyx mori serine protease homolog BmSPH-1 regulates nodule melanization. Here, we show the dual role of BmSPH-1 in the development and immunity of B. mori . BmSPH-1 was expressed in hemocytes after molting and during the larval-pupal transformation in normal development. In contrast, following infection, BmSPH-1 was expressed in hemocytes and cleaved in the hemolymph, which resulted in the induction of PO activity. Moreover, BmSPH-1 was cleaved in the cuticle during the larval-pupal transformation and early pupal stages. In BmSPH-1 RNAi-treated silkworms, the reduced BmSPH-1 mRNA levels during the spinning stage or the prepupal stage resulted in the arrest of pupation or pupal cuticular melanization, respectively. The binding assays revealed that BmSPH-1 interacts with B. mori immulectin, proPO, and proPO-activating enzyme. Our findings demonstrate that BmSPH-1 paticipates larval-pupal transformation, pupal cuticular melanization and innate immunity of silkworms, illustrating the dual role of BmSPH-1 in development and immunity. Highlights: Bombyx mori serine protease homolog BmSPH-1 functions in both development and immunity. BmSPH-1 acts in the immune response during infection. BmSPH-1 is required for pupation during the larval-pupal transformation. BmSPH-1 participates in pupal cuticular melanization. BmSPH-1 interacts with BmIML, BmPPAE, and BmPPOs. … (more)
- Is Part Of:
- Developmental and comparative immunology. Volume 85(2018)
- Journal:
- Developmental and comparative immunology
- Issue:
- Volume 85(2018)
- Issue Display:
- Volume 85, Issue 2018 (2018)
- Year:
- 2018
- Volume:
- 85
- Issue:
- 2018
- Issue Sort Value:
- 2018-0085-2018-0000
- Page Start:
- 170
- Page End:
- 176
- Publication Date:
- 2018-08
- Subjects:
- Bombyx mori -- Development -- Immunity -- Serine protease homolog -- Silkworm
Immunology -- Periodicals
Developmental immunology -- Periodicals
616.079 - Journal URLs:
- http://www.sciencedirect.com/science/journal/0145305X ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.dci.2018.04.011 ↗
- Languages:
- English
- ISSNs:
- 0145-305X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3579.051000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 6454.xml